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Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules
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Zeitschriftentitel: | Molecular Biology of the Cell |
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Personen und Körperschaften: | , , , , , , , |
In: | Molecular Biology of the Cell, 18, 2007, 4, S. 1385-1396 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
American Society for Cell Biology (ASCB)
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Schlagwörter: |
author_facet |
Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia |
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author |
Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia |
spellingShingle |
Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia Molecular Biology of the Cell Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules Cell Biology Molecular Biology |
author_sort |
nonhoff, ute |
spelling |
Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e06-12-1120 <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules Molecular Biology of the Cell |
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10.1091/mbc.e06-12-1120 |
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American Society for Cell Biology (ASCB), 2007 |
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title |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_unstemmed |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_full |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_fullStr |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_full_unstemmed |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_short |
Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_sort |
ataxin-2 interacts with the dead/h-box rna helicase ddx6 and interferes with p-bodies and stress granules |
topic |
Cell Biology Molecular Biology |
url |
http://dx.doi.org/10.1091/mbc.e06-12-1120 |
publishDate |
2007 |
physical |
1385-1396 |
description |
<jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> |
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author | Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia |
author_facet | Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia, Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia |
author_sort | nonhoff, ute |
container_issue | 4 |
container_start_page | 1385 |
container_title | Molecular Biology of the Cell |
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description | <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> |
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spelling | Nonhoff, Ute Ralser, Markus Welzel, Franziska Piccini, Ilaria Balzereit, Daniela Yaspo, Marie-Laure Lehrach, Hans Krobitsch, Sylvia 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e06-12-1120 <jats:p>Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.</jats:p> Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules Molecular Biology of the Cell |
spellingShingle | Nonhoff, Ute, Ralser, Markus, Welzel, Franziska, Piccini, Ilaria, Balzereit, Daniela, Yaspo, Marie-Laure, Lehrach, Hans, Krobitsch, Sylvia, Molecular Biology of the Cell, Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules, Cell Biology, Molecular Biology |
title | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_full | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_fullStr | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_full_unstemmed | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_short | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
title_sort | ataxin-2 interacts with the dead/h-box rna helicase ddx6 and interferes with p-bodies and stress granules |
title_unstemmed | Ataxin-2 Interacts with the DEAD/H-Box RNA Helicase DDX6 and Interferes with P-Bodies and Stress Granules |
topic | Cell Biology, Molecular Biology |
url | http://dx.doi.org/10.1091/mbc.e06-12-1120 |